MGST1_HUMAN
ID MGST1_HUMAN Reviewed; 155 AA.
AC P10620; A8K533; G5EA53;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Microsomal glutathione S-transferase 1;
DE Short=Microsomal GST-1;
DE EC=2.5.1.18;
DE AltName: Full=Microsomal GST-I;
GN Name=MGST1; Synonyms=GST12, MGST;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=3372534; DOI=10.1016/s0021-9258(18)68495-9;
RA Dejong J.L., Morgenstern R., Joernvall H., Depierre J.W., Tu C.-P.D.;
RT "Gene expression of rat and human microsomal glutathione S-transferases.";
RL J. Biol. Chem. 263:8430-8436(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Foreskin;
RX PubMed=8812420; DOI=10.1006/geno.1996.0429;
RA Kelner M.J., Stokely M.N., Stovall N.E., Montoya M.A.;
RT "Structural organization of the human microsomal glutathione S-transferase
RT gene (GST12).";
RL Genomics 36:100-103(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10524215; DOI=10.1016/s0167-4781(99)00112-8;
RA Lee S.H., DeJong J.;
RT "Microsomal GST-I: genomic organization, expression, and alternative
RT splicing of the human gene.";
RL Biochim. Biophys. Acta 1446:389-396(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Prostate;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Conjugation of reduced glutathione to a wide number of
CC exogenous and endogenous hydrophobic electrophiles. Has a wide
CC substrate specificity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=glutathione + RX = a halide anion + an S-substituted
CC glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC ChEBI:CHEBI:90779; EC=2.5.1.18;
CC -!- ACTIVITY REGULATION: Can be activated by reagents that attack Cys-50
CC sulfhydryl, such as N-ethylmaleimide. Activation also occurs via
CC nitration of Tyr-93 by peroxynitrite (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotrimer; The trimer binds only one molecule of glutathione.
CC {ECO:0000250}.
CC -!- INTERACTION:
CC P10620; P01133: EGF; NbExp=3; IntAct=EBI-2691601, EBI-640857;
CC P10620; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-2691601, EBI-12175685;
CC P10620; O75084: FZD7; NbExp=3; IntAct=EBI-2691601, EBI-746917;
CC P10620; Q8WX92: NELFB; NbExp=2; IntAct=EBI-2691601, EBI-347721;
CC P10620; Q96PQ1: SIGLEC12; NbExp=3; IntAct=EBI-2691601, EBI-17640454;
CC P10620; O14798: TNFRSF10C; NbExp=3; IntAct=EBI-2691601, EBI-717441;
CC P10620; P01282-2: VIP; NbExp=3; IntAct=EBI-2691601, EBI-12320391;
CC -!- SUBCELLULAR LOCATION: Microsome {ECO:0000250}. Mitochondrion outer
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P10620-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P10620-2; Sequence=VSP_046160;
CC -!- TISSUE SPECIFICITY: Highly expressed in liver.
CC -!- PTM: Peroxynitrite induces nitration at Tyr-93 which activates the
CC enzyme. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MAPEG family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/mgst1/";
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DR EMBL; J03746; AAA35934.1; -; mRNA.
DR EMBL; U46498; AAC50711.1; -; Genomic_DNA.
DR EMBL; AF092926; AAC50711.1; JOINED; Genomic_DNA.
DR EMBL; U46497; AAC50711.1; JOINED; Genomic_DNA.
DR EMBL; U71213; AAB17184.1; -; Genomic_DNA.
DR EMBL; U71211; AAB17184.1; JOINED; Genomic_DNA.
DR EMBL; U71212; AAB17184.1; JOINED; Genomic_DNA.
DR EMBL; BT006982; AAP35628.1; -; mRNA.
DR EMBL; AY368173; AAQ55111.1; -; Genomic_DNA.
DR EMBL; AK291148; BAF83837.1; -; mRNA.
DR EMBL; AC007528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007529; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC007552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471094; EAW96362.1; -; Genomic_DNA.
DR EMBL; CH471094; EAW96367.1; -; Genomic_DNA.
DR EMBL; BC005923; AAH05923.1; -; mRNA.
DR EMBL; BC056863; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS58209.1; -. [P10620-2]
DR CCDS; CCDS8677.1; -. [P10620-1]
DR PIR; B28083; B28083.
DR RefSeq; NP_001247440.1; NM_001260511.1. [P10620-1]
DR RefSeq; NP_001247441.1; NM_001260512.1.
DR RefSeq; NP_001254527.1; NM_001267598.1. [P10620-2]
DR RefSeq; NP_064696.1; NM_020300.4. [P10620-1]
DR RefSeq; NP_665707.1; NM_145764.2. [P10620-1]
DR RefSeq; NP_665734.1; NM_145791.2. [P10620-1]
DR RefSeq; NP_665735.1; NM_145792.2. [P10620-1]
DR AlphaFoldDB; P10620; -.
DR SMR; P10620; -.
DR BioGRID; 110413; 122.
DR IntAct; P10620; 36.
DR MINT; P10620; -.
DR STRING; 9606.ENSP00000379512; -.
DR BindingDB; P10620; -.
DR ChEMBL; CHEMBL1743184; -.
DR DrugBank; DB00143; Glutathione.
DR DrugBank; DB03310; Glutathione disulfide.
DR GlyGen; P10620; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P10620; -.
DR MetOSite; P10620; -.
DR PhosphoSitePlus; P10620; -.
DR SwissPalm; P10620; -.
DR BioMuta; MGST1; -.
DR DMDM; 121740; -.
DR EPD; P10620; -.
DR jPOST; P10620; -.
DR MassIVE; P10620; -.
DR MaxQB; P10620; -.
DR PaxDb; P10620; -.
DR PeptideAtlas; P10620; -.
DR PRIDE; P10620; -.
DR ProteomicsDB; 34143; -.
DR ProteomicsDB; 52620; -. [P10620-1]
DR TopDownProteomics; P10620-1; -. [P10620-1]
DR Antibodypedia; 23831; 235 antibodies from 32 providers.
DR DNASU; 4257; -.
DR Ensembl; ENST00000010404.6; ENSP00000010404.2; ENSG00000008394.13. [P10620-1]
DR Ensembl; ENST00000396207.1; ENSP00000379510.1; ENSG00000008394.13. [P10620-1]
DR Ensembl; ENST00000396209.5; ENSP00000379512.1; ENSG00000008394.13. [P10620-1]
DR Ensembl; ENST00000396210.8; ENSP00000379513.3; ENSG00000008394.13. [P10620-1]
DR Ensembl; ENST00000535309.5; ENSP00000438308.1; ENSG00000008394.13. [P10620-2]
DR GeneID; 4257; -.
DR KEGG; hsa:4257; -.
DR MANE-Select; ENST00000396210.8; ENSP00000379513.3; NM_020300.5; NP_064696.1.
DR UCSC; uc001rdf.4; human. [P10620-1]
DR CTD; 4257; -.
DR DisGeNET; 4257; -.
DR GeneCards; MGST1; -.
DR HGNC; HGNC:7061; MGST1.
DR HPA; ENSG00000008394; Tissue enhanced (adipose tissue, adrenal gland, liver).
DR MIM; 138330; gene.
DR neXtProt; NX_P10620; -.
DR OpenTargets; ENSG00000008394; -.
DR PharmGKB; PA30791; -.
DR VEuPathDB; HostDB:ENSG00000008394; -.
DR eggNOG; ENOG502S0BD; Eukaryota.
DR GeneTree; ENSGT00390000011980; -.
DR HOGENOM; CLU_105467_1_0_1; -.
DR InParanoid; P10620; -.
DR OMA; TFSMAYN; -.
DR PhylomeDB; P10620; -.
DR TreeFam; TF105327; -.
DR PathwayCommons; P10620; -.
DR Reactome; R-HSA-156590; Glutathione conjugation.
DR Reactome; R-HSA-5423646; Aflatoxin activation and detoxification.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P10620; -.
DR BioGRID-ORCS; 4257; 12 hits in 1088 CRISPR screens.
DR ChiTaRS; MGST1; human.
DR GeneWiki; Microsomal_glutathione_S-transferase_1; -.
DR GenomeRNAi; 4257; -.
DR Pharos; P10620; Tbio.
DR PRO; PR:P10620; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; P10620; protein.
DR Bgee; ENSG00000008394; Expressed in right adrenal gland and 185 other tissues.
DR ExpressionAtlas; P10620; baseline and differential.
DR Genevisible; P10620; HS.
DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; ISS:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005778; C:peroxisomal membrane; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0004602; F:glutathione peroxidase activity; IDA:UniProtKB.
DR GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
DR GO; GO:0071449; P:cellular response to lipid hydroperoxide; IDA:UniProtKB.
DR GO; GO:0034635; P:glutathione transport; IDA:UniProtKB.
DR Gene3D; 1.20.120.550; -; 1.
DR InterPro; IPR023352; MAPEG-like_dom_sf.
DR InterPro; IPR001129; Membr-assoc_MAPEG.
DR InterPro; IPR040162; MGST1-like.
DR PANTHER; PTHR10689; PTHR10689; 1.
DR Pfam; PF01124; MAPEG; 1.
DR SUPFAM; SSF161084; SSF161084; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Endoplasmic reticulum; Membrane;
KW Microsome; Mitochondrion; Mitochondrion outer membrane; Nitration;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..155
FT /note="Microsomal glutathione S-transferase 1"
FT /id="PRO_0000217736"
FT TOPO_DOM 3..9
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 10..33
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 34..62
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 63..96
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 97..99
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT TRANSMEM 100..123
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 124..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250"
FT TRANSMEM 129..148
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TOPO_DOM 149..155
FT /note="Lumenal"
FT /evidence="ECO:0000250"
FT BINDING 38
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 73
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 74
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 81
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT BINDING 121
FT /ligand="glutathione"
FT /ligand_id="ChEBI:CHEBI:57925"
FT /evidence="ECO:0000250"
FT SITE 50
FT /note="Activates the enzyme when modified"
FT /evidence="ECO:0000250"
FT MOD_RES 42
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VS7"
FT MOD_RES 55
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VS7"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91VS7"
FT VAR_SEQ 75..155
FT /note="AHLNDLENIIPFLGIGLLYSLSGPDPSTAILHFRLFVGARIYHTIAYLTPLP
FT QPNRALSFFVGYGVTLSMAYRLLKSKLYL -> IKQTLSIYLASSI (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_046160"
SQ SEQUENCE 155 AA; 17599 MW; 892A529C97E3C853 CRC64;
MVDLTQVMDD EVFMAFASYA TIILSKMMLM STATAFYRLT RKVFANPEDC VAFGKGENAK
KYLRTDDRVE RVRRAHLNDL ENIIPFLGIG LLYSLSGPDP STAILHFRLF VGARIYHTIA
YLTPLPQPNR ALSFFVGYGV TLSMAYRLLK SKLYL
